IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. J. Biol. Chem. (0021-9258) 2011 imex curation Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com 23-Sept-2011: Contacted by JYOTI. orchard Only protein-protein interactions human-hec1a Homo sapiens hec1a human endometrial carcinoma cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis no aa@gene.com Accepted 2011-AUG-05 by ORCHARD 23-Sept-2011: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2011 orchard Only protein-protein interactions imex curation TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. J. Biol. Chem. (0021-9258) 2011 imex curation Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com 23-Sept-2011: Contacted by JYOTI. orchard Only protein-protein interactions human-hec1a Homo sapiens hec1a human endometrial carcinoma cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com Accepted 2011-AUG-05 by ORCHARD 23-Sept-2011: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2011 orchard Only protein-protein interactions imex curation TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. J. Biol. Chem. (0021-9258) 2011 imex curation Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com 23-Sept-2011: Contacted by JYOTI. orchard Only protein-protein interactions human-hsc3 Homo sapiens hsc3 Human oral squamous carcinoma cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis no aa@gene.com Accepted 2011-AUG-05 by ORCHARD 23-Sept-2011: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2011 orchard Only protein-protein interactions imex curation TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. J. Biol. Chem. (0021-9258) 2011 imex curation Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com 23-Sept-2011: Contacted by JYOTI. orchard Only protein-protein interactions human-hsc3 Homo sapiens hsc3 Human oral squamous carcinoma cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ikner A., Ashkenazi A. Apoptosis - Interactions involving proteins with a function related to apoptosis aa@gene.com Accepted 2011-AUG-05 by ORCHARD 23-Sept-2011: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2011 orchard Only protein-protein interactions imex curation tnr12_human Tumor necrosis factor receptor superfamily member 12A TNFRSF12A FN14 Fibroblast growth factor-inducible immediate-early response protein 14 Tweak-receptor protein protein human Homo sapiens Human MARGSLRRLLRLLVLGLWLALLRSVAGEQAPGTAPCSRGSSWSADLDKCMDCASCRARPHSDFCLGCAAAPPAPFRLLWPILGGALSLTFVLGLLSGFLVWRRCRRREKFTTPIEETGGEGCPAVALIQ BF3FDFB9C1E1C448 fadd_human FAS-associated death domain protein FAS-associating death domain-containing protein Mediator of receptor induced toxicity FADD MORT1 GIG3 Growth-inhibiting gene 3 protein protein protein human Homo sapiens Human MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS DIP protein Q13158 original sequence version: 155 DIP protein Q13158 original sequence version: 130 DIP protein Q13158 original sequence version: 110 DIP protein Q13158 original sequence version: 118 DIP protein Q13158 original sequence version: 141 DIP protein Q13158 original sequence version: 166 0E65E2F852E83507 ripk1_human Receptor-interacting serine/threonine-protein kinase 1 RIPK1 RIP Cell death protein RIP RIP1 Receptor-interacting protein 1 protein protein human Homo sapiens Human MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVVKRMQSLQLDCVAVPSSRSNSATEQPGSLHSSQGLGMGPVEESWFAPSLEHPQEENEPSLQSKLQDEANYHLYGSRMDRQTKQQPRQNVAYNREEERRRRVSHDPFAQQRPYENFQNTEGKGTAYSSAASHGNAVHQPSGLTSQPQVLYQNNGLYSSHGFGTRPLDPGTAGPRVWYRPIPSHMPSLHNIPVPETNYLGNTPTMPFSSLPPTDESIKYTIYNSTGIQIGAYNYMEIGGTSSSLLDSTNTNFKEEPAAKYQAIFDNTTSLTDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLLSSLIYVSQN DIP protein Q13546 original sequence version: 158 DIP protein Q13546-1 original sequence version: 140 DIP protein Q13546 original sequence version: 146 DIP protein Q13546-1 original sequence version: 146 DIP protein Q13546 original sequence version: 134 DIP protein Q13546 original sequence version: 109 976E2428D525A9B2 casp8_human Caspase-8 CASP8 MCH5 ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog FADD-homologous ICE/ced-3-like protease FADD-like ICE Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 protein protein human Homo sapiens Human MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD DIP protein Q14790 original sequence version: 184 DIP protein Q14790 original sequence version: 135 DIP protein Q14790 original sequence version: 136 DIP protein Q14790 original sequence version: 147 DIP protein Q14790 original sequence version: 146 DIP protein Q14790 original sequence version: 170 DIP protein Q14790 original sequence version: 198 DIP protein Q14790-1 original sequence version: 197 DIP protein Q14790 original sequence version: 158 7A5FEAA6B39B582F birc2_human Baculoviral IAP repeat-containing protein 2 Inhibitor of apoptosis protein 2 TNFR2-TRAF-signaling complex protein 2 IAP homolog B RING finger protein 48 BIRC2 API1 MIHB RNF48 RING-type E3 ubiquitin transferase BIRC2 Cellular inhibitor of apoptosis 1 protein protein human Homo sapiens Human MHKTASQRLFPGPSYQNIKSIMEDSTILSDWTNSNKQKMKYDFSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKLGDSPIQKHKQLYPSCSFIQNLVSASLGSTSKNTSPMRNSFAHSLSPTLEHSSLFSGSYSSLSPNPLNSRAVEDISSSRTNPYSYAMSTEEARFLTYHMWPLTFLSPSELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPNCPFLENSLETLRFSISNLSMQTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEFLIRMKGQEFVDEIQGRYPHLLEQLLSTSDTTGEENADPPIIHFGPGESSSEDAVMMNTPVVKSALEMGFNRDLVKQTVQSKILTTGENYKTVNDIVSALLNAEDEKREEEKEKQAEEMASDDLSLIRKNRMALFQQLTCVLPILDNLLKANVINKQEHDIIKQKTQIPLQARELIDTILVKGNAAANIFKNCLKEIDSTLYKNLFVDKNMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDKEVSVVFIPCGHLVVCQECAPSLRKCPICRGIIKGTVRTFLS C1778D328063586D traf2_human TNF receptor-associated factor 2 TRAF2 TRAP3 Tumor necrosis factor type 2 receptor-associated protein 3 E3 ubiquitin-protein ligase TRAF2 RING-type E3 ubiquitin transferase TRAF2 protein protein human Homo sapiens Human MAAASVTPPGSLELLQPGFSKTLLGTKLEAKYLCSACRNVLRRPFQAQCGHRYCSFCLASILSSGPQNCAACVHEGIYEEGISILESSSAFPDNAARREVESLPAVCPSDGCTWKGTLKEYESCHEGRCPLMLTECPACKGLVRLGEKERHLEHECPERSLSCRHCRAPCCGADVKAHHEVCPKFPLTCDGCGKKKIPREKFQDHVKTCGKCRVPCRFHAIGCLETVEGEKQQEHEVQWLREHLAMLLSSVLEAKPLLGDQSHAGSELLQRCESLEKKTATFENIVCVLNREVERVAMTAEACSRQHRLDQDKIEALSSKVQQLERSIGLKDLAMADLEQKVLEMEASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL DIP protein Q12933 original sequence version: 131 DIP protein Q12933 original sequence version: 129 DIP protein Q12933 original sequence version: 167 DIP protein Q12933 original sequence version: 193 DIP protein Q12933-1 original sequence version: 154 DIP protein Q12933 original sequence version: 130 DIP protein Q12933 original sequence version: 151 C508BE185B783B20 tnfrsf12a-birc2 4 9 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait living cell living cell physical association physical association Fig. 2a TWEAK (O43508) is required for the interaction to happen. tnfrsf12a-traf2 4 5 unspecified role unspecified role bait bait living cell living cell 10 unspecified role unspecified role prey prey physical association physical association Fig 2b TWEAK (O43508) is required for the interaction to happen. tnfrsf12a-birc2-2 2 9 unspecified role unspecified role prey prey FN14 5 unspecified role unspecified role bait bait living cell living cell 10 unspecified role unspecified role prey prey association association Fig. S3 TWEAK (O43508) is required for the interaction to happen. casp8-ripk1 3 7 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait physical association physical association Figs. 3a, 5a and 7e TWEAK (O43508) is required for the interaction to happen. FADD knock-down decreases the CASP8-RIP1K interaction (fig. 3e). TNFR1 knock-down decreases the CASP8-RIP1K interaction (fig. 5a). TNFR1:Fc antagonist blocks TWEAK-induced CASP8-FADD-RIP1K interaction (fig. 5f). CYLD knock-down disrupts TWEAK-induced CASP8-FADD-RIP1K interaction (Fig. 6c). traf2-tnfrsf12a-1 4 10 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey living cell living cell physical association physical association Fig. 2c TWEAK (O43508) is required for the interaction to happen. casp8-ripk1-6 1 8 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey physical association physical association Fig. S4 TWEAK (O43508) is required for the interaction to happen. ripk1-casp8 4 6 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 8 unspecified role unspecified role prey prey association association Fig. 3b TWEAK (O43508) is required for the interaction to happen. TNR12 knock-down disrupts the interaction (fig. S5). casp8-fadd-9 4 8 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey 6 unspecified role unspecified role prey prey association association Fig. 3e, 5f, 6a and 6c TWEAK (O43508) is required for the interaction to happen. TNR12 knock-down disrupts the interaction (fig. S5). CYLD knock-down disrupts the interaction (fig. 6c).